Collaboration Teams - Members share responsibility for posting refined answers to the guided readings - succinct, relevant, clear, and with pictures or a video to compliment.
When contributing to the reading guide, follow these steps: 1) First complete the reading guide on your own from the chemistry unit page. 2) Write your response to a question in word and then copy it. Be sure to upload pictures and/or video for each question. 3) Click on the edit button and then go to the appropriate question and paste your answer below it.Sign your contribution with your first name and last initial and TEAM COLOR 4) Scroll to the very bottom and in the Optional comment box, place a summary of what you did and sign it (e.g. "I answered chp 26 question 3" - Tom S.) Then click Save.
Blue
Purple
Green
Pink
Yellow
Orange
Red
Shayne
Laura
Steven
Martin
Corrine
Emily
Kim
Jordan
Jared
Mario
Alyssa
Zach
Brian
Sean
Jackie
Sawyer
Dan
Keely
Illian
Jim
Amanda
Adam Steph
16-18
14-15
11-13
9-10
6-8
4-5, 20
1-3, 19
Chapter 5 Guided Reading Assignment 1.Upload pictures/videos of a monomer, polymer, condensation reaction, and hydrolysis. Explain each with example.
Hydrolosis Condensation Reaction
2.What is a glycosidic linkage and what do the numbers 1-4 and 1-2 relate to?
Glycosidic linkage is a covalent bond formed between two monosaccharides by a dehydration reaction. And the numbers tell which carbons are linked.
3. Compare and contrast the two storage polysaccharides. 1) Starch: a polymer of plants that consists of all glucose monomers, mostly joined by 1-4 linkages.
2) Glycogen: a polymer of animals, stored in liver and muscle cells, that is a more extensively-branched polymer of glucose.
-Amanda P. 4.Compare and contrast the two structural polysaccharides. Chitin is a structural polysaccharide in the exoskeletons of animals.It forms a leathery material, but is hard when in a salty environment.Fungi use chitin to build cell walls.It contains nitrogen.All glucose molecules face the same direction.
Cellulose is used by plants to make cell walls. It contains no nitrogen.The glucose molecules’ orientation alternates.
5.Why are lipids grouped together as a family of molecules? All lipids are hydrophobic (dislike water), and are composed of hydrocarbons.
Sawyer W
6.What are the building blocks of fats and how do they combine?
I helped with Triglyceride formation
Fats are made up of two kinds of smaller molecules by dehydration reactions. These small molecules are glycerol and fatty acids. Glycerols are made up of alcohol with three carbons, each becoming a hydroxyl group. The fatty acids have a long carbon skeleton (16-18 carbon atoms long). At one end there is a carboxyl group and long hydrocarbon chains. Fats combine by (Jackie and Sean I need you guys help on this part). -- Brian N. the Yellow Team
7.Contrast saturated and unsaturated fats – how does this relate to the concept that structure and function (how they are used by living things) are linked? Saturated-- It is when in hydrocarbon chains of fatty acids, there are no double bonds between carbon atoms and they have as many hydrogen atoms as they can. They are straight and packed closer together than unsaturated fats, causing them to be solid at room temperature; this is the bad types of fat.
Unsaturated-- It is when in hydrocarbon chains of fatty acids, there are one or more double bonds of carbon and they have less hydrogen atoms than in saturated fats. There will be a kink in the chain where the “cis” or “trans” double bond is. These unsaturated fats are less tightly packed and as a result liquid at room temperature; this is the better types of fats for you.
This helps further relate the fact that structure and function are linked because with that small kink there is less room for it to be tightly packed: being a liquid. Also the solid (saturated) fats contribute to many heart and other diseases; there will be too much fats in the blood veins that can build up like plaque.
-- Brian N. the Yellow Team
8. Upload a picture of a phospoholipid and label significant functional groups. -- Brian N. the Yellow Team
9. How would you recognize a basic steroid molecule? Steroids can be characterized by a carbon skeleton that has four fused rings.Different steroids are characterized by the different functional groups attached to the rings.
Zack B.
10. upload pictures of the eight types of proteins and their basic function.
Protein
Function
Enzymatic Proteins
Selective acceleration of chemical reactions
Structural Proteins
Support
Storage proteins
Storage of amino acids
Transport Proteins
Transport of other substances
Hormonal Proteins
Coordination of an organism’s activity
Receptor Proteins
Response of cell to chemical stimuli
Contractile and Motor Proteins
Movement
Defensive Proteins
Protection against disease
Zack B.
11. What are the names for the monomers and polymers of proteins? The monomers of proteins are called amino acids and the polymers are called polypeptides.
amino acids
polypeptides 12. Upload a video of the catalytic cycle of an enzyme – and then describe a real world example.
Score on this video!
In the body the enzyme sucrase accelerates hydrolysis of sucrose into glucose and fructose. The sucrase protein is not consumed during the cycle, and it can be used again for further catalysis. 13. upload pictures of two amino acids – note the amino group, the carboxyl group and the alpha carbon, circle the water molecule to be removed and then note the peptide bond formed when the two are joined.
14. Explain the four levels of protein structure – Include pictures a.Primary: unique sequence of amino acids; for example, the order of letters in a very long word
b.Secondary: coils and folds in the polypeptide chain which are the result of hydrogen bonds between the repeating constituents of the polypeptide backbone. This includes a helix ( a delicate coil held together by hydrogen bonding between every 4th amino acid) and a pleated sheet (2 or more regions of the polypeptide chain laying side by side are connected by hydrogen bonds between parts of the 2 parallel polypeptide backbones.)
c.Tertiary: the overall shape of a polypeptide resulting from interactions between the side chains of various amino acids. Hydrophobic chains end up in clusters at the core of the protein and other interactions begin to occur, giving the whole protein a unique shape.
d.Quaternary: overall protein structure that results from the aggregation of polypeptide subunits. This happens when proteins consist of 2 or more polypeptide chains aggregated into one functional macromolecule.
15. How does the characteristics of an amino acid – nonpolar, polar, acidic or basic relate to the issue of tertiary and quaternary structure?
The different characteristics of amino acids are determined by their side chains. The configurations of the side chains determine whether the carboxyl group is nonpolar, polar, acidic, or basic. The side chains can make an entire amino acid hydrophobic, hydrophilic, negatively charged, or positively charged. The characteristics of the side chain also determine what kind of reactions the amino acid will be able to have and what it can bond with. The type of chain that is formed due the characteristics of individual amino acids determines the type of structure that amino acids will form together to create a protein.
16. What does denaturation mean and why is it important? Provide an everyday example.
If the pH, salt concentration, temperature, or other aspects of its environment are altered, the protein may unravel and lose its native conformation, which is a change called denaturation. Because it is misshapen, the denatured protein is biologically inactive. Most proteins become denatured if they are transferred from an aqueous environment to an organic solvent.
17. What are chaperonins and what is their role in protein structure?
Chaperonins are protein molecules that assist the proper folding of other proteins. Chaperonins do not actually specify the correct final structure of a polypeptide. Instead they work by keeping the new polypeptide segregated from "bad influences" in the cytoplasmic environment while it folds spontaneously.
18. Describe the technique of x-ray crystallography. It’s used to determine a protein’s three-dimensional structure. Researchers aim an X-ray beam through the crystallized protein. The atoms of the crystal deflect the X-rays into an orderly array. The diffracted X-rays expose photographic film, producing a pattern of spots known as an X-ray diffraction pattern. Using data from these, scientists build a 3D computer model of the protein.
19. What are the roles of nucleic acids?
Nucleic acid allows organisms ability to reproduce complex components from one gereration to the next.
DNA
RNA 20. Upload a picture of DNA that includes significant labels and explain what is meant by the term that DNA is antiparallel? The ''antiparallel" term when describing
DNA refers to the double helix. The strands of the double helix are organized in opposite orientation, so that the 5’ end of one strand is aligned with the 3’ end of the other.
Collaboration Teams - Members share responsibility for posting refined answers to the guided readings - succinct, relevant, clear, and with pictures or a video to compliment.
When contributing to the reading guide, follow these steps:
1) First complete the reading guide on your own from the chemistry unit page.
2) Write your response to a question in word and then copy it. Be sure to upload pictures and/or video for each question.
3) Click on the edit button and then go to the appropriate question and paste your answer below it. Sign your contribution with your first name and last initial and TEAM COLOR
4) Scroll to the very bottom and in the Optional comment box, place a summary of what you did and sign it (e.g. "I answered chp 26 question 3" - Tom S.) Th en click Save.
Laura
Steven
Corrine
Emily
Jordan
Jared
Alyssa
Zach
Sean
Jackie
Dan
Keely
Illian
Amanda
Adam
Steph
Chapter 5 Guided Reading Assignment
1.Upload pictures/videos of a monomer, polymer, condensation reaction, and hydrolysis. Explain each with example.
2.What is a glycosidic linkage and what do the numbers 1-4 and 1-2 relate to?
Glycosidic linkage is a covalent bond formed between two monosaccharides by a dehydration reaction. And the numbers tell which carbons are linked.
3. Compare and contrast the two storage polysaccharides.
1) Starch: a polymer of plants that consists of all glucose monomers, mostly joined by 1-4 linkages.
2) Glycogen: a polymer of animals, stored in liver and muscle cells, that is a more extensively-branched polymer of glucose.
-Amanda P.
4.Compare and contrast the two structural polysaccharides.
Chitin is a structural polysaccharide in the exoskeletons of animals. It forms a leathery material, but is hard when in a salty environment. Fungi use chitin to build cell walls. It contains nitrogen. All glucose molecules face the same direction.
Cellulose is used by plants to make cell walls. It contains no nitrogen. The glucose molecules’ orientation alternates.
5.Why are lipids grouped together as a family of molecules?
All lipids are hydrophobic (dislike water), and are composed of hydrocarbons.
Sawyer W
6.What are the building blocks of fats and how do they combine?
Fats are made up of two kinds of smaller molecules by dehydration reactions. These small molecules are glycerol and fatty acids. Glycerols are made up of alcohol with three carbons, each becoming a hydroxyl group. The fatty acids have a long carbon skeleton (16-18 carbon atoms long). At one end there is a carboxyl group and long hydrocarbon chains. Fats combine by (Jackie and Sean I need you guys help on this part).
-- Brian N. the Yellow Team
7.Contrast saturated and unsaturated fats – how does this relate to the concept that structure and function (how they are used by living things) are linked?
Saturated-- It is when in hydrocarbon chains of fatty acids, there are no double bonds between carbon atoms and they have as many hydrogen atoms as they can. They are straight and packed closer together than unsaturated fats, causing them to be solid at room temperature; this is the bad types of fat.
Unsaturated-- It is when in hydrocarbon chains of fatty acids, there are one or more double bonds of carbon and they have less hydrogen atoms than in saturated fats. There will be a kink in the chain where the “cis” or “trans” double bond is. These unsaturated fats are less tightly packed and as a result liquid at room temperature; this is the better types of fats for you.
This helps further relate the fact that structure and function are linked because with that small kink there is less room for it to be tightly packed: being a liquid. Also the solid (saturated) fats contribute to many heart and other diseases; there will be too much fats in the blood veins that can build up like plaque.
-- Brian N. the Yellow Team
8. Upload a picture of a phospoholipid and label significant functional groups.
-- Brian N. the Yellow Team
9. How would you recognize a basic steroid molecule?
Steroids can be characterized by a carbon skeleton that has four fused rings. Different steroids are characterized by the different functional groups attached to the rings.
Zack B.
10. upload pictures of the eight types of proteins and their basic function.
Zack B.
11. What are the names for the monomers and polymers of proteins?
The monomers of proteins are called amino acids and the polymers are called polypeptides.
12. Upload a video of the catalytic cycle of an enzyme – and then describe a real world example.
In the body the enzyme sucrase accelerates hydrolysis of sucrose into glucose and fructose. The sucrase protein is not consumed during the cycle, and it can be used again for further catalysis.
13. upload pictures of two amino acids – note the amino group, the carboxyl group and the alpha carbon, circle the water molecule to be removed and then note the peptide bond formed when the two are joined.
14. Explain the four levels of protein structure – Include pictures
a.Primary:
unique sequence of amino acids; for example, the order of letters in a very long word
b.Secondary:
coils and folds in the polypeptide chain which are the result of hydrogen bonds between the repeating constituents of the polypeptide backbone. This includes a helix ( a delicate coil held together by hydrogen bonding between every 4th amino acid) and a pleated sheet (2 or more regions of the polypeptide chain laying side by side are connected by hydrogen bonds between parts of the 2 parallel polypeptide backbones.)
c.Tertiary:
the overall shape of a polypeptide resulting from interactions between the side chains of various amino acids. Hydrophobic chains end up in clusters at the core of the protein and other interactions begin to occur, giving the whole protein a unique shape.
d.Quaternary:
overall protein structure that results from the aggregation of polypeptide subunits. This happens when proteins consist of 2 or more polypeptide chains aggregated into one functional macromolecule.
15. How does the characteristics of an amino acid – nonpolar, polar, acidic or basic relate to the issue of tertiary and quaternary structure?
The different characteristics of amino acids are determined by their side chains. The configurations of the side chains determine whether the carboxyl group is nonpolar, polar, acidic, or basic. The side chains can make an entire amino acid hydrophobic, hydrophilic, negatively charged, or positively charged. The characteristics of the side chain also determine what kind of reactions the amino acid will be able to have and what it can bond with. The type of chain that is formed due the characteristics of individual amino acids determines the type of structure that amino acids will form together to create a protein.
16. What does denaturation mean and why is it important? Provide an everyday example.
If the pH, salt concentration, temperature, or other aspects of its environment are altered, the protein may unravel and lose its native conformation, which is a change called denaturation. Because it is misshapen, the denatured protein is biologically inactive. Most proteins become denatured if they are transferred from an aqueous environment to an organic solvent.
17. What are chaperonins and what is their role in protein structure?
Chaperonins are protein molecules that assist the proper folding of other proteins. Chaperonins do not actually specify the correct final structure of a polypeptide. Instead they work by keeping the new polypeptide segregated from "bad influences" in the cytoplasmic environment while it folds spontaneously.
18. Describe the technique of x-ray crystallography.
It’s used to determine a protein’s three-dimensional structure. Researchers aim an X-ray beam through the crystallized protein. The atoms of the crystal deflect the X-rays into an orderly array. The diffracted X-rays expose photographic film, producing a pattern of spots known as an X-ray diffraction pattern. Using data from these, scientists build a 3D computer model of the protein.
19. What are the roles of nucleic acids?
Nucleic acid allows organisms ability to reproduce complex components from one gereration to the next.
DNA
RNA
20. Upload a picture of DNA that includes significant labels and explain what is meant by the term that DNA is antiparallel?
DNA refers to the double helix. The strands of the double helix are organized in opposite orientation, so that the 5’ end of one strand is aligned with the 3’ end of the other.
Dan